Alterations in DNA-dependent RNA polymerase I from rat liver accompanying ethionine administration

1982 ◽  
Vol 105 (3) ◽  
pp. 799-805 ◽  
Author(s):  
Haruko Yamano ◽  
Yasuko Sawai ◽  
Wen Long Thung ◽  
Fumiyasu Sato ◽  
Kinji Tsukada
Biochemistry ◽  
1975 ◽  
Vol 14 (22) ◽  
pp. 4907-4911 ◽  
Author(s):  
Joseph Martial ◽  
Josefina Zaldivar ◽  
Paulina Bull ◽  
Alejandro Venegas ◽  
Pablo Valenzuela

1986 ◽  
Vol 235 (3) ◽  
pp. 699-705 ◽  
Author(s):  
H Matsui ◽  
H Yazawa ◽  
N Suzuki ◽  
T Hosoya

The activity of the template-engaged form of RNA polymerase I from livers of adrenalectomized rats was about 50-60% of that of normal control rats, and increased about 2-fold at 6 h after the administration of dexamethasone. However, no change was found in the activity of the ‘free’ form of RNA polymerase I or the template-engaged form of RNA polymerase II. Immunochemical studies using guinea-pig anti-(RNA polymerase I) serum disclosed that the total number of RNA polymerase I molecules did not vary during the treatment with dexamethasone. Cycloheximide caused a rapid decrease in the template-engaged form of RNA polymerase I activity in normal rats and in dexamethasone-treated (6 h) adrenalectomized rats, to the value in adrenalectomized rats, but affected it only slightly in adrenalectomized rats. The elongation rate of rRNA-precursor synthesis in liver nuclei was not affected by a change in the concentration of circulating dexamethasone. From these results, it is concluded that about half the rRNA-precursor synthesis in rat liver is regulated by glucocorticoids, probably through the synthesis of short-lived protein(s) which may play a role in conversion of the ‘dormant’ form of RNA polymerase I into the ‘engaged’ form.


AGE ◽  
1983 ◽  
Vol 6 (4) ◽  
pp. 106-112 ◽  
Author(s):  
Patricia Fitzpatrick-Dimond ◽  
John A. Todhunter ◽  
Sameeh S. Elridi

1982 ◽  
Vol 2 (3) ◽  
pp. 155-161 ◽  
Author(s):  
Fu-Li Yu ◽  
Annabella Barrett

Rat-liver nucleoli (10–15 pg DNA) were digested with either 0.6 or 3 units of DNase I for various times (up to 1 h). RNA synthesis was then measured in the absence or presence ol 3 units of Escherichia coli RNA polymerase. It was found that the nucleolar chromatin supporting the endogenous engaged RNA polymerase I transcription was compl-etely destroyed in 3 min with either concentration of DNase I. The nucleolar chromatin template transcribed by E. coli RNA polymerase retained 50% of its original capacity even 60 min alter 3 units of DNase I digestion. When hybridization experiments were conducted, it was found that the DNAs derived from both levels of DNase-Idigested nucleoli were incapable of forming hybrids with the labelled nucleolar RNA synthesized by the engaged RNA polymerase I from the untreated nucleoli. Since the engaged RNA polymerase I transcribes only the physiologically active genes of the nucleolar chromatin, and the RNA transcripts represent active gene product, these data suggest that DNase I digestion has completely destroyed the active genes of the nucleolar chromatin, and E. coli RNA polymerase is able to transcribe the inactive nucleolar chromatin template.


Biochemistry ◽  
1977 ◽  
Vol 16 (8) ◽  
pp. 1655-1665 ◽  
Author(s):  
Michael I. Goldberg ◽  
Jean Claude Perriard ◽  
William J. Rutter

1987 ◽  
Vol 241 (1) ◽  
pp. 169-174 ◽  
Author(s):  
M Urata ◽  
N Suzuki ◽  
T Hosoya

In order to examine the relationship between RNA polymerase I and ornithine decarboxylase (ODC), three lines of experiments were performed, with the following results. The glucocorticoid-induced increase of RNA polymerase I in rat liver nuclei was not abolished by administration of inhibitors of ODC synthesis and activity, namely 1,3-diaminopropane and 2-difluoromethylornithine respectively. Anti-ODC antibody did not cross-react with RNA polymerase I solubilized from rat liver nucleoli, indicating the absence of a common protein sequence in these enzymes. The ODC preparation which was treated with transglutaminase in the presence of putrescine could not stimulate the activity of RNA polymerase I in nuclei of liver and prostate. All these results suggest that the increases in ODC protein or activity are not a prerequisite to the increase in RNA polymerase I after hormonal or physiological stimuli, but rather that the increases in both enzymes are separate responses to the primary stimuli.


Author(s):  
John A. Todhunter ◽  
Michael Tainsky ◽  
Herbert Weissbach ◽  
Nathan Brot

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